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1.  Phage as a source of antibacterial genes 
Bacteriophage  2011;1(4):195-197.
Bacteriophage-encoded proteins which inhibit or modify cellular components may contribute to antibacterial drug discovery by allowing the identification of novel targets. Given their abundance and diversity, phages may have various strategies in host inhibition and therefore may possess a variety of such proteins. Using Rhodococcus equi and phage YF1, we show that a single phage possesses numerous genes that inhibit the host when introduced into the host on a plasmid. These genes mostly encode proteins of unknown function, confirming the potential that this approach may have in providing new antibacterial targets.
doi:10.4161/bact.1.4.17746
PMCID: PMC3448104  PMID: 23050212
antibacterial drug discovery; bactericidal proteins; multidrug resistance; phage YF1; target identification
2.  Pathogenic Nocardia, Rhodococcus, and Related Organisms Are Highly Susceptible to Imidazole Antifungals 
Rhodococcus equi and species of Nocardia and Gordonia may be human opportunistic pathogens. We find that these, as well as several isolates from closely related genera, are highly susceptible to the imidazoles bifonazole, clotrimazole, econazole, and miconazole, whose MICs are ≤1 μg/ml. In liquid cultures 1 μg of the drug/ml was bacteriostatic and 10 μg/ml was bactericidal. On solid media at 10 μg of azole/ml no resistant mutants could be isolated. An MIC of 1 to 15 μg/ml was observed with ketoconazole, whereas none of these organisms was inhibited by the triazoles fluconazole and voriconazole (100 μg/ml). Imidazoles may offer the prospect of treatment of nocardioform mycetomas and may provide the basis for the development of additional antimicrobial agents to combat these pathogens.
doi:10.1128/AAC.47.4.1476-1478.2003
PMCID: PMC152489  PMID: 12654698
3.  Cloning, Sequencing, and Characterization of the Hexahydro-1,3,5-Trinitro-1,3,5-Triazine Degradation Gene Cluster from Rhodococcus rhodochrous 
Applied and Environmental Microbiology  2002;68(10):4764-4771.
Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) is a high explosive which presents an environmental hazard as a major land and groundwater contaminant. Rhodococcus rhodochrous strain 11Y was isolated from explosive contaminated land and is capable of degrading RDX when provided as the sole source of nitrogen for growth. Products of RDX degradation in resting-cell incubations were analyzed and found to include nitrite, formaldehyde, and formate. No ammonium was excreted into the medium, and no dead-end metabolites were observed. The gene responsible for the degradation of RDX in strain 11Y is a constitutively expressed cytochrome P450-like gene, xplA, which is found in a gene cluster with an adrenodoxin reductase homologue, xplB. The cytochrome P450 also has a flavodoxin domain at the N terminus. This study is the first to present a gene which has been identified as being responsible for RDX biodegradation. The mechanism of action of XplA on RDX is thought to involve initial denitration followed by spontaneous ring cleavage and mineralization.
doi:10.1128/AEM.68.10.4764-4771.2002
PMCID: PMC126434  PMID: 12324318
4.  ADP-Ribosylation as an Intermediate Step in Inactivation of Rifampin by a Mycobacterial Gene 
Mycobacterium smegmatis DSM43756 inactivates rifampin, and the inactivated antibiotic product recovered from culture medium was ribosylated on the 23-OH group. To study this process, the gene responsible for the inactivation was expressed at high levels by the lac promoter in Escherichia coli conferring resistance to >500 μg of antibiotic per ml. Cell homogenates generated a novel derivative designated RIP-TAs; in this study, we determined that RIP-TAs is 23-(O-ADP-ribosyl)rifampin. Our results indicated that RIP-TAs is an intermediate in the pathway leading to ribosylated rifampin and that the previously characterized gene encodes a mono(ADP-ribosyl)transferase which, however, shows no sequence similarity to other enzymes of this class.
PMCID: PMC89045  PMID: 9869590
5.  Escherichia coli Kasugamycin Dependence Arising from Mutation at the rpsI Locus 
Journal of Bacteriology  1983;153(2):709-715.
Escherichia coli mutants with alterations in the electrophoretic mobility of ribosomal protein S9 were used to locate rpsI, the gene for this protein, on the linkage map. rpsI was located at about 70 min, roughly halfway between argG and fabE. It was very close to the gene for ribosomal protein L13, rplM. Another mutation at the rpsI locus gave rise to a phenotype of kasugamycin dependence and resistance. In this mutant, dependence on antibiotic came from kasugamycin being necessary to slow the rate of protein synthesis.
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PMCID: PMC221688  PMID: 6337124
6.  The Gene for Ribosomal Protein L13, rplM, Is Located Near argR, at About 70 Minutes on the Escherichia coli Chromosomal Linkage Map 
Journal of Bacteriology  1982;149(2):779-782.
Mutants of Escherichia coli with alterations in the electrophoretic mobility of ribosomal protein L13 were used to locate rplM, the gene for this protein, on the chromosomal linkage map. rplM was situated between gltB and argR, at about 70 min.
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PMCID: PMC216573  PMID: 7035437

Results 1-6 (6)